RGD Reference Report - Inhibition of protein phosphatase-1 is linked to phosphorylation of p53 and apoptosis. - Rat Genome Database

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Inhibition of protein phosphatase-1 is linked to phosphorylation of p53 and apoptosis.

Authors: Long, X  Wu, G  Gaa, ST  Rogers, TB 
Citation: Long X, etal., Apoptosis 2002 Feb;7(1):31-9.
RGD ID: 1299086
Pubmed: PMID:11773703   (View Abstract at PubMed)

p53 is a multifunctional protein and its activity can be modulated by phosphorylation and dephosphorylation. In this study, we sought to examine the notion that serine/threonine phosphatases (PP-1 and PP-2A) are active modulators of the p53-dependent apoptotic pathway. Exposure of neonatal rat cardiomyocytes to the established apoptotic agents, bafilomycin A1 (BAF) or staurosporine (STAU) induced apoptosis and caused a decrease in PP-1 activity of 35%. This response was restricted to apoptotic stimuli as treatment with phenylephrine neither decreased PP-1 and PP-2A activity nor induced DNA fragmentation in cardiomyocytes. The level of phosphorylated p53 was increased as a result of BAF or STAU-treatment. We further examined the effect of PP-1 inhibition on cardiomyocytes by the use of the phosphatase inhibitor, okadaic acid, and an antisense strategy. Okadaic acid (100 nM) resulted in a decrease in PP-1 activity of 45%, enhanced phosphorylation of p53, and stimulated apoptosis. Furthermore, overexpression of the antisense PP-1 catalytic subunit transcript caused a 44% decrease in expression of PP-1, with no change in the levels of the PP-2A catalytic subunit, and also evoked DNA fragmentation. Our data support the view that decreased activity of PP-1 is an important signaling event in the apoptotic process.

Objects referenced in this article
Gene Tp53 tumor protein p53 Rattus norvegicus

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